First enzymological characterization of selenocysteine β-lyase from a lactic acid bacterium, Leuconostoc mesenteroides.
Lactic acid bacteria
Leuconostoc mesenteroides
Selenium metabolism
Selenocysteine β-lyase
Journal
Amino acids
ISSN: 1438-2199
Titre abrégé: Amino Acids
Pays: Austria
ID NLM: 9200312
Informations de publication
Date de publication:
May 2022
May 2022
Historique:
received:
15
10
2021
accepted:
20
01
2022
pubmed:
6
2
2022
medline:
9
6
2022
entrez:
5
2
2022
Statut:
ppublish
Résumé
We succeeded in expressing selenocysteine β-lyase (SCL) from a lactic acid bacterium, Leuconostoc mesenteroides LK-151 (Lm-SCL), in the soluble fractions of Escherichia coli Rosetta (DE3) using a novel expression vector of pET21malb constructed by ourselves that has both maltose binding protein (MBP)- and 6 × His-tag. Lm-SCL acted on L-selenocysteine, L-cysteine, and L-cysteine sulfinic acid but showed a high preference for L-selenocysteine. The k
Identifiants
pubmed: 35122135
doi: 10.1007/s00726-022-03133-9
pii: 10.1007/s00726-022-03133-9
doi:
Substances chimiques
Selenoproteins
0
Selenocysteine
0CH9049VIS
Lactic Acid
33X04XA5AT
Lyases
EC 4.-
selenocysteine lyase
EC 4.4.1.16
Cysteine
K848JZ4886
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
787-798Informations de copyright
© 2022. The Author(s), under exclusive licence to Springer-Verlag GmbH Austria, part of Springer Nature.
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